Epstein-Barr virus (EBV) Latent Membrane Protein 2A (LMP2A) is a transmembrane protein essential for viral latency and immune evasion, structured with distinct functional domains. The N-terminal domain modulates B-cell receptor signaling, while the transmembrane and C-terminal regions help anchor the protein and facilitate additional interactions within host cells. This study characterizes the LMP2A C-terminal domain (CTD) structure under various conditions using CD spectroscopy and NMR. The 29-residue C-tail sequence contains key residues that impact stability. CD analysis shows that, while disordered at neutral pH and in water, helicity is slightly enhanced under acidic conditions and membrane-mimicking environments, with DTT influencing stability through oxidation state effects. NMR structural analysis in DPC micelles reveals a well-converged helical structure extending from residues R471 to E486, closely matching AlphaFold predictions. The data highlight the CTD's structural plasticity and suggest roles for cysteines and hydrophobic clusters in stabilizing the peptide in membrane-like settings.

The binding feature of bipyrrole-strapped calix[4]pyrrole 1 for the fluoride anion was examined by a combination of ¹H and ¹⁹F NMR spectroscopy in DMSO-d₆ . Receptor 1 was found to bind the fluoride anion with high affinity via two step-process. Fluoride binding to receptor 1 was proved to facilitate deuterium exchange of the pyrrolic protons in the nominally aprotic deuterated solvent of DMSO-d₆.

The peptide hormone glucagon has served as both a biopharmaceutical agent for clinical use and a model peptide forming amyloid fibrils. As we recently established a recombinant production of glucagon, its backbone NMR assignments at neutral pHs were conducted in the present study. However, as the NMR spectra showed severe line broadening and poor dispersion at pHs 7.5 and 7.0, complete backbone NMR assignments could be obtained at pH 6.0. Interestingly, CSI and TALOS predictions using the assigned chemical shift values indicated different probabilities of secondary structure. These results suggest that glucagon would adopt an unusual or dynamically fluctuating conformation in solution. Therefore, detailed conformation and molecular dynamics of glucagon would be worthy of investigation, for which the present results provide an experimental basis.

This article presents various features related to a strange, yet extremely important group of proteins called intrinsically disordered proteins (IDPs) which used to be and are still by some called generically "unstructured" proteins. Huge abundance (~30% of the entire human proteome) of IDPs has brought a critical paradigm shift in protein science as well as in structural biology during the last three decades. In this article a brief introduction on these unorthodox proteins will be followed by an explanation for "the long-and-winding" journey to reach the consensus name of IDP. The term IDP was adopted with difficulty only in 2012 after 20 years since the first discovery reports on "unstructured" proteins had appeared. Next, some comments will be made on the hurdles encountered in the early days to have the concept of "unstructured" proteins or the manuscripts dealing with them accepted in the protein science field. Thirdly, the saga by the KRIBB NMR team to establish the pre-structured motifs (PreSMos) that are the transient secondary structures observed in the target unbound state of IDPs as the target-binding active sites of IDPs will be delineated in depth along with the relevant publications. Finally, the issues that need to be explored further in the IDP field such as AlphaFold will be discussed.

Based on projected Liouville equation, we theoretically investigated the magnetic field dependence of the magneto-optical cyclotron transition of the quasi two-dimensional Landau splitting system in GaAs and CdS. Through the numerical analysis of the current work, we found the increasing properties of line-widths of GaAs and CdS with magnetic field. We also found that line-widths of GaAs < CdS in the magnetic field region of B > 20.06 T and presented the reasonable resonating pictures of the line-widths.

Fluoxetine, a selective serotonin reuptake inhibitor (SSRI), enhances serotonin levels in synapses to alleviate depressive symptoms. This study investigates the effects of fluoxetine on the aquatic organism Daphnia magna (D. magna), known for its environmental sensitivity. D. magna was exposed to 100 ㎍/L of fluoxetine for 72 hours, and metabolomic changes were examined using high-resolution magic angle spinning (HR-MAS) NMR. A total of twenty-eight metabolites were identified. Compared to the control group, fluoxetine exposure resulted in decreased levels of phenylalanine and increased levels of sn-glycero- 3-phosphocholine, inosine, proline, carnosine, and tryptophan.